Rabbit kidney aminopeptidases: purification and some properties

Rabbit kidney aminopeptidases: purification and some properties

Autor Oliveira, S. M. Google Scholar
Freitas, J. O. Google Scholar
Alves, K. B. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo Aminopeptidases (EC.3.4.11...) are widely distributed in nature and have medical and biological importance due to their function in the modification and degradation of protein. Two aminopeptidases were purified from rabbit kidney homogenate by ion exchange and gel filtration chromatography columns, using aminoacyl of beta-naphthylamides and p-nitroanilides as substrates. the enzymes' homogeneity was assured by SDS-PAGE. the first enzyme (P-1) has an optimum of pH 7.0, a molecular mass of 70 kDa, best catalytical efficiency for methionyl-beta-naphthylamide, is 70% inhibited by 0.5 mM Zn2+ and Co2+ ions, 3.33 mM sodium hydrocortisone succinate and 0.08 mM p-hydroxymercuribenzoate, and is little or not inhibited by EDTA, amino acids, p-nitroaniline, beta-naphthylamine, deoxicholate, bestatin and puromycin. the second enzyme (P-2) has an optimum of pH 7.0, a molecular mass of 54 kDa, best catalytical efficiency for Leu-beta-naphthylamide, is inhibited by 0.5 mM ions Zn2+ (45%), 0.02 mM EDTA (94%) 0.08 mM p-hydroxymercuribenzoate (70%), 3.33 mM beta-ME (13%), 1.33 mM p-nitroaniline (40%), 1.33 mM beta-naphthylamine (17%), 1.33 mM sodium deoxicholate (96%), 3.33 mM sodium hydrocortisone succinate (60%), and is 30% activated by 0.5 mM Co2+ ions. Puromycin and bestatin are competitive inhibitors with K-i values in 10(-6) and 10(-7) M order, respectively. P-1 is a methionine aminopeptidase, while P-2 is a leucine aminopeptidase. (C) 1999 Elsevier Science B.V. All rights reserved.
Palavra-chave rabbit kidney
aminopeptidase
arylamidase
arylaminopeptidase
rabbit
Idioma Inglês
Data de publicação 1999-12-01
Publicado em Immunopharmacology. Amsterdam: Elsevier B.V., v. 45, n. 1-3, p. 215-221, 1999.
ISSN 0162-3109 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 215-221
Fonte http://dx.doi.org/10.1016/S0162-3109(99)00080-6
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000084080100034
Endereço permanente http://repositorio.unifesp.br/handle/11600/26189

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